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Host protein

6-Phospho-gluconolactonase (6-PGLac) A2A adenosine receptor Adipocyte lipid binding protein (ALBP) Antibody Antibody 03-1 Antibody 12E11G Antibody 13G10 Antibody 13G10 / 14H7 Antibody 14H7 Antibody 1G8 Antibody 28F11 Antibody 38C2 Antibody 3A3 Antibody 7A3 Antibody7G12-A10-G1-A12 Antibody L-chain from Mab13-1 hybridoma cells Antibody SN37.4 Apo-[Fe]-hydrogenase from M. jannaschii Apo-ferritin Apo-HydA1 ([FeFe]-hydrogenase) from C. reinhardtii Apo-HydA enzymes from C. reinhardtii, M. elsdenii, C. pasteurianum Artificial construct Avidin (Av) Azurin Binding domain of Rabenosyn (Rab4) Bovine carbonic anhydrase (CA) Bovine carbonic anhydrase II (CA) Bovine serum albumin (BSA) Bovine β-lactoglobulin (βLG) Bromelain Burkavidin C45 (c-type cytochrome maquette) Carbonic anhydrase (CA) Carboxypeptidase A Catabolite activator protein (CAP) CeuE C-terminal domain of calmodulin Cutinase Cytochrome b562 Cytochrome BM3h Cytochrome c Cytochrome c552 Cytochrome cb562 Cytochrome c peroxidase Cytochrome P450 (CYP119) Domain of Hin recombinase Due Ferro 1 E. coli catabolite gene activator protein (CAP) [FeFe]-hydrogenase from C. pasteurianum (CpI) Ferredoxin (Fd) Ferritin FhuA FhuA ΔCVFtev Flavodoxin (Fld) Glyoxalase II (Human) (gp27-gp5)3 gp45 [(gp5βf)3]2 Heme oxygenase (HO) Hemoglobin Horse heart cytochrome c Horseradish peroxidase (HRP) Human carbonic anhydrase Human carbonic anhydrase II (hCAII) Human retinoid-X-receptor (hRXRa) Human serum albumin (HSA) HydA1 ([FeFe]-hydrogenase) from C. reinhardtii IgG 84A3 Laccase Lipase B from C. antarctica (CALB) Lipase from G. thermocatenulatus (GTL) LmrR Lysozyme Lysozyme (crystal) Mimochrome Fe(III)-S6G(D)-MC6 (De novo designed peptide) Mouse adenosine deaminase Myoglobin (Mb) Neocarzinostatin (variant 3.24) NikA Nitrobindin (Nb) Nitrobindin variant NB4 Nuclease from S. aureus Papain (PAP) Photoactive Yellow Protein (PYP) Photosystem I (PSI) Phytase Prolyl oligopeptidase (POP) Prolyl oligopeptidase (POP) from P. furiosus Rabbit serum albumin (RSA) Ribonuclease S RNase A Rubredoxin (Rd) Silk fibroin fibre Small heat shock protein from M. jannaschii ß-lactoglobulin Staphylococcal nuclease Steroid Carrier Protein 2L (SCP 2L) Sterol Carrier Protein (SCP) Streptavidin (monmeric) Streptavidin (Sav) Thermolysin Thermosome (THS) tHisF TM1459 cupin TRI peptide Trypsin Tryptophan gene repressor (trp) Xylanase A (XynA) Zn8:AB54 Zn8:AB54 (mutant C96T) α3D peptide α-chymotrypsin β-lactamase β-lactoglobulin (βLG)

Corresponding author

Akabori, S. Alberto, R. Albrecht, M. Anderson, J. L. R. Apfel, U.-P. Arnold, F. H. Artero, V. Bäckvall, J. E. Baker, D. Ball, Z. T. Banse, F. Berggren, G. Bian, H.-D. Birnbaum, E. R. Borovik, A. S. Bren, K. L. Bruns, N. Brustad, E. M. Cardona, F. Case, M. A. Cavazza, C. Chan, A. S. C. Coleman, J. E. Craik, C. S. Creus, M. Cuatrecasas, P. Darnall, D. W. DeGrado, W. F. Dervan, P. B. de Vries, J. Diéguez, M. Distefano, M. D. Don Tilley, T. Duhme-Klair, A. K. Ebright, R. H. Emerson, J. P. Eppinger, J. Fasan, R. Filice, M. Fontecave, M. Fontecilla-Camps, J. C. Fruk, L. Fujieda, N. Fussenegger, M. Gademann, K. Gaggero, N. Germanas, J. P. Ghattas, W. Ghirlanda, G. Golinelli-Pimpaneau, B. Goti, A. Gras, E. Gray, H. B. Green, A. P. Gross, Z. Gunasekeram, A. Happe, T. Harada, A. Hartwig, J. F. Hasegawa, J.-Y. Hayashi, T Hemschemeier, A. Herrick, R. S. Hilvert, D. Hirota, S. Huang, F.-P. Hureau, C. Hu, X. Hyster, T. K. Imanaka, T. Imperiali, B. Itoh, S. Janda, K. D. Jarvis, A. G. Jaussi, R. Jeschek, M. Kaiser, E. T. Kamer, P. C. J. Kazlauskas, R. J. Keinan, E. Khare, S. D. Kim, H. S. Kitagawa, S. Klein Gebbink, R. J. M. Kokubo, T. Korendovych, I. V. Kuhlman, B. Kurisu, G. Laan, W. Lee, S.-Y. Lehnert, N. Leow, T. C. Lerner, R. A. Lewis, J. C. Liang, H. Lindblad, P. Lin, Y.-W. Liu, J. Lombardi, A. Lubitz, W. Lu, Y. Maglio, O. Mahy, J.-P. Mangiatordi, G. F. Marchetti, M. Maréchal, J.-D. Marino, T. Marshall, N. M. Matile, S. Matsuo, T. McNaughton, B. R. Ménage, S. Messori, L. Mulfort, K. L. Nastri, F. Nicholas, K. M. Niemeyer, C. M. Nolte, R. J. M. Novič, M. Okamoto, Y. Okano, M. Okuda, J. Onoda, A. Oohora, K. Palomo, J. M. Pàmies, O. Panke, S. Pan, Y. Paradisi, F. Pecoraro, V. L. Pordea, A. Reetz, M. T. Reijerse, E. Renaud, J.-L. Ricoux, R. Rimoldi, I. Roelfes, G. Rovis, T. Sakurai, S. Salmain, M. Sasaki, T. Sauer, D. F. Schultz, P. G. Schwaneberg, U. Seelig, B. Shafaat, H. S. Shahgaldian, P. Sheldon, R. A. Shima, S. Sigman, D. S. Song, W. J. Soumillion, P. Strater, N. Sugiura, Y. Szostak, J. W. Tezcan, F. A. Thorimbert, S. Tiede, D. M. Tiller, J. C. Turner, N. J. Ueno, T. Utschig, L. M. van Koten, G. Wang, J. Ward, T. R. Watanabe, Y. Whitesides, G. M. Wilson, K. S. Woolfson, D. N. Yilmaz, F. Zhang, J.-L.

Journal

3 Biotech Acc. Chem. Res. ACS Catal. ACS Cent. Sci. ACS Sustainable Chem. Eng. Adv. Synth. Catal. Angew. Chem., Int. Ed. Appl. Biochem. Biotechnol. Appl. Organomet. Chem. Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications Beilstein J. Org. Chem. Biochemistry Biochim. Biophys. Acta, Bioenerg. Biochimie Bioconjug. Chem. Bioorg. Med. Chem. Bioorg. Med. Chem. Lett. Bioorganometallic Chemistry: Applications in Drug Discovery, Biocatalysis, and Imaging Biopolymers Biotechnol. Adv. Biotechnol. Bioeng. Can. J. Chem. Catal. Lett. Catal. Sci. Technol. Cat. Sci. Technol. ChemBioChem ChemCatChem Chem. Commun. Chem. Rev. Chem. Sci. Chem. Soc. Rev. Chem. - Eur. J. Chem. - Asian J. Chem. Lett. ChemistryOpen ChemPlusChem Chimia Commun. Chem. Comprehensive Inorganic Chemistry II Comprehensive Supramolecular Chemistry II C. R. Chim. Coordination Chemistry in Protein Cages: Principles, Design, and Applications Coord. Chem. Rev. Croat. Chem. Acta Curr. Opin. Biotechnol. Curr. Opin. Chem. Biol. Curr. Opin. Struct. Biol. Dalton Trans. Effects of Nanoconfinement on Catalysis Energy Environ. Sci. Eur. J. Biochem. Eur. J. Inorg. Chem. FEBS Lett. Helv. Chim. Acta Inorg. Chim. Acta Inorg. Chem. Int. J. Mol. Sci. Isr. J. Chem. J. Biol. Chem. J. Biol. Inorg. Chem. J. Immunol. Methods J. Inorg. Biochem. J. Mol. Catal. A: Chem. J. Mol. Catal. B: Enzym. J. Organomet. Chem. J. Phys. Chem. Lett. J. Porphyr. Phthalocyanines J. Protein Chem. J. Am. Chem. Soc. J. Chem. Soc. J. Chem. Soc., Chem. Commun. Methods Enzymol. Mol. Divers. Molecular Encapsulation: Organic Reactions in Constrained Systems Nature Nat. Catal. Nat. Chem. Biol. Nat. Chem. Nat. Commun. Nat. Protoc. Nat. Rev. Chem. New J. Chem. Org. Biomol. Chem. Plos ONE Proc. Natl. Acad. Sci. U. S. A. Process Biochem. Prog. Inorg. Chem. Prot. Eng. Protein Engineering Handbook Protein Expression Purif. Pure Appl. Chem. RSC Adv. Science Small Synlett Tetrahedron Tetrahedron: Asymmetry Tetrahedron Lett. Chem. Rec. Top. Catal. Top. Organomet. Chem. Trends Biotechnol.

A De Novo Designed Metalloenzyme for the Hydration of CO2

Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature’s approach to catalysis, a ZnII metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single‐stranded three‐helix bundle and binds ZnII with high affinity using His3O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400‐fold of the fastest carbonic anhydrase isoform, CAII, and 11‐fold of CAIII.

Metal:

Zn

Ligand type:

Amino acid

Host protein:

α3D peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM ≈ 3.8*104 M-1*s-1

A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers

Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O2 to H2O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

1056

ee:

---

PDB:

4FWX

Notes:

Sperm whale myoglobin

A Designed Heme-[4Fe-4S] Metalloenzyme Catalyzes Sulfite Reduction like the Native Enzyme

Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved—through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites—to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts, this study provides strategies for designing highly functional multicofactor artificial enzymes.

Metal:

Fe

Host protein:

Cytochrome c peroxidase

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Sulfite reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

Designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase

A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O2 reduction rate (52 s–1) comparable to that of a native cytochrome (cyt) cbb3 oxidase (50 s–1) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional oxidase model designed in sperm whale myoglobin and its native redox partner, cyt b5, resulting in a 400-fold electron transfer (ET) rate enhancement. Achieving high activity equivalent to that of native enzymes in a designed metalloenzyme offers deeper insight into the roles of tunable processes such as ET in oxidase activity and enzymatic function and may extend into applications such as more efficient oxygen reduction reaction catalysts for biofuel cells.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

O2 reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

O2 reduction rates of 52 s-1 were achieved in combination with the native redox partner cyt b5.

A Designed Supramolecular Protein Assembly with In Vivo Enzymatic Activity

The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(kcat/Km)/kuncat] for ampicillin hydrolysis of 2.3 × 106 and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions.

Metal:

Zn

Ligand type:

Amino acid

Host protein:

Cytochrome cb562

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

4U9E

Notes:

---

A Hydrogenase Model System Based on the Sequence of Cytochrome c: Photochemical Hydrogen Evolution in Aqueous Media

The diiron carbonyl cluster is held by a native CXXC motif, which includes Cys14 and Cys17, in the cytochrome c sequence. It is found that the diiron carbonyl complex works well as a catalyst for H2 evolution. It has a TON of ∼80 over 2 h at pH 4.7 in the presence of a Ru-photosensitizer and ascorbate as a sacrificial reagent in aqueous media.

Metal:

Fe

Ligand type:

Carbonyl

Host protein:

Cytochrome c

Anchoring strategy:

Dative

Optimization:

---

Reaction:

H2 evolution

Max TON:

82

ee:

---

PDB:

---

Notes:

Horse heart cytochrome C

Alteration of the Oxygen-Dependent Reactivity of De Novo Due Ferri Proteins

De novo proteins provide a unique opportunity to investigate the structure–function relationships of metalloproteins in a minimal, well-defined and controlled scaffold. Here, we describe the rational programming of function in a de novo designed di-iron carboxylate protein from the Due Ferri family. Originally created to catalyse the O2-dependent, two-electron oxidation of hydroquinones, the protein was reprogrammed to catalyse the selective N-hydroxylation of arylamines by remodelling the substrate access cavity and introducing a critical third His ligand to the metal-binding cavity. Additional second- and third-shell modifications were required to stabilize the His ligand in the core of the protein. These structural changes resulted in at least a 106-fold increase in the relative rate between the arylamine N-hydroxylation and hydroquinone oxidation reactions. This result highlights the potential for using de novo proteins as scaffolds for future investigations of the geometric and electronic factors that influence the catalytic tuning of di-iron active sites.

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

N-Hydroxylation

Max TON:

---

ee:

---

PDB:

2LFD

Notes:

---

An Artificial Di-Iron Oxo-Orotein with Phenol Oxidase Activity

Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site.

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Alcohol oxidation

Max TON:

>50

ee:

---

PDB:

2KIK

Notes:

kcat/KM ≈ 1380 M-1*min-1

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Amine oxidation

Max TON:

---

ee:

---

PDB:

2KIK

Notes:

kcat/KM ≈ 83 M-1*min-1

An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein

Guided by nature: A designed binding site comprising the His/His/Asp motif for CuII complexation has been constructed in a robust protein by site‐specific mutagenesis (see picture). The artificial metalloenzyme catalyzes an enantioselective Diels–Alder reaction.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

tHisF

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

6.7

ee:

46

PDB:

---

Notes:

---

Aqueous Light Driven Hydrogen Production by a Ru–Ferredoxin–Co Biohybrid

Metal:

Co

Ligand type:

Oxime

Host protein:

Ferredoxin (Fd)

Anchoring strategy:

Dative

Optimization:

---

Reaction:

H2 evolution

Max TON:

210

ee:

---

PDB:

---

Notes:

Recalculated TON

Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo- b-lactamase into a Catechol Oxidase

Metal:

Cu

Ligand type:

Amino acid

Host protein:

β-lactamase

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Catechol oxidation

Max TON:

---

ee:

---

PDB:

2FU7

Notes:

---

A Structural View of Synthetic Cofactor Integration into [FeFe]-Hydrogenases

Metal:

Fe

Ligand type:

CN; CO; Dithiolate

Anchoring strategy:

Dative

Optimization:

Chemical

Reaction:

H2 evolution

Max TON:

---

ee:

---

PDB:

4XDC

Notes:

H2 evolution activity of the ArM: 2874 (mmol H2)*min-1*(mg protein)-1.

Building Reactive Copper Centers in Human Carbonic Anhydrase II

Metal:

Cu

Ligand type:

Amino acid

Anchoring strategy:

Dative

Optimization:

---

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

1RZC

Notes:

Oxidation of 2-aminophenol with subsequent formation of 2-aminophenoxazinone. Reaction rate = 0.09 s-1

Carbene in Cupredoxin Protein Scaffolds: Replacement of a Histidine Ligand in the Active Site Substantially Alters Copper Redox Properties

Metal:

Cu

Host protein:

Azurin

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Electron transfer

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Carbonic Anhydrase II as Host Protein for the Creation of a Biocompatible Artificial Metathesase

Metal:

Ru

Ligand type:

Carbene

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Olefin metathesis

Max TON:

28

ee:

---

PDB:

---

Notes:

Ring closing metathesis. 28 turnovers obtained under physiological conditions within 4 hours.

Catalysis by a De Novo Zinc-Mediated Protein Interface: Implications for Natural Enzyme Evolution and Rational Enzyme Engineering

Metal:

Zn

Ligand type:

Amino acid

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>50

ee:

---

PDB:

3V1C

Notes:

---

Catalytic Reduction of NO to N2O by a Designed Heme Copper Center in Myoglobin: Implications for the Role of Metal Ions

Metal:

Cu

Ligand type:

Amino acid; Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

2400

ee:

---

PDB:

---

Notes:

Sperm whale myoglobin

Chalcogenide Substitution in the [2Fe] Cluster of [FeFe]-Hydrogenases Conserves High Enzymatic Activity

Metal:

Fe

Ligand type:

CN; CO; Diselenolate

Anchoring strategy:

Dative

Optimization:

Chemical

Reaction:

H2 evolution

Max TON:

---

ee:

---

PDB:

5OEF

Notes:

---

Computational Redesign of a Mononuclear Zinc Metalloenzyme for Organophosphate Hydrolysis

Metal:

Zn

Ligand type:

Amino acid

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

>140

ee:

---

PDB:

3T1G

Notes:

kcat/KM ≈ 104 M-1*s-1

Control of the Coordination Structure of Organometallic Palladium Complexes in an Apo-Ferritin Cage

Metal:

Pd

Ligand type:

Allyl

Host protein:

Ferritin

Anchoring strategy:

Dative

Optimization:

---

Reaction:

Suzuki coupling

Max TON:

---

ee:

---

PDB:

2ZG7

Notes:

---

Defining the Role of Tyrosine and Rational Tuning of Oxidase Activity by Genetic Incorporation of Unnatural Tyrosine Analogs

Metal:

Cu

Ligand type:

Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

1200

ee:

---

PDB:

4FWX

Notes:

Sperm whale myoglobin

Definite Coordination Arrangement of Organometallic Palladium Complexes Accumulated on the Designed Interior Surface of Apo-Ferritin

Metal:

Pd

Ligand type:

Allyl

Host protein:

Ferritin

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Suzuki coupling

Max TON:

---

ee:

---

PDB:

---

Notes:

---

De Novo Design of Catalytic Proteins

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Alcohol oxidation

Max TON:

>100

ee:

---

PDB:

---

Notes:

kcat/KM ≈ 1540 M-1*min-1

Design and Evolution of New Catalytic Activity with an Existing Protein Scaffold

Metal:

Zn

Ligand type:

Amino acid

Host protein:

Glyoxalase II (Human)

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

2F50

Notes:

kcat/KM ≈ 184 M-1*s-1

Designing a Functional Type 2 Copper Center that has Nitrite Reductase Activity Within α-Helical Coiled Coils

Metal:

Cu

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>5

ee:

---

PDB:

---

Notes:

Nitrite reduction

Design of a Switchable Eliminase

Metal:

Ca

Ligand type:

Amino acid

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Kemp elimination

Max TON:

>40

ee:

---

PDB:

2KZ2

Notes:

Ca acts as allosteric regulator, catalytically active site contains no metal

Diruthenium Diacetate-Catalyzed Aerobic Oxidation of Hydroxylamines and Improved Chemoselectivity by Immobilization to Lysozyme

Metal:

Ru

Ligand type:

Amino acid; OAc

Host protein:

Lysozyme

Anchoring strategy:

Dative

Optimization:

Chemical

Max TON:

1000

ee:

---

PDB:

---

Notes:

---

Engineered Metal Regulation of Trypsin Specificity

Metal:

Zn

Ligand type:

Amino acid

Host protein:

Trypsin

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Substrate specificty

Metal:

Ni

Ligand type:

Amino acid

Host protein:

Trypsin

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Substrate specificty

Hybrid [FeFe]-Hydrogenases with Modified Active Sites Show Remarkable Residual Enzymatic Activity

Metal:

Fe

Ligand type:

CN; CO; Dithiolate

Anchoring strategy:

Dative

Optimization:

Chemical

Max TON:

---

ee:

---

PDB:

---

Notes:

H2 evolution: TOF = 450 s-1. H2 oxidation: TOF = 150 s-1.

Hydrolytic Catalysis and Structural Stabilization in a Designed Metalloprotein

Metal:

Hg; Zn

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>10

ee:

---

PDB:

3PBJ

Notes:

Zn ion for catalytic activity, Hg ion for structural stability of the ArM. PDB ID 3PBJ = Structure of an analogue.

Metal:

Hg; Zn

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

3PBJ

Notes:

Zn ion for catalytic activity, Hg ion for structural stability of the ArM, kcat/KM ≈ 1.8*105 M-1*s-1. PDB ID 3PBJ = Structure of an analogue.